In the work presented here, a photocatalytic system using titanium Degussa P-25 in suspension was used to evaluate the degradation of 20mg L(-1) of antibiotic oxolinic acid (OA). The effects of catalyst load (0.2-1.5 g L(-1)) and pH (7.5-11) were evaluated and optimized using the surface response methodology and the Pareto diagram. In the range of variables studied, low pH values and 1.0 g L(-1) of TiO(2) favoured the efficiency of the process. Under optimal conditions the evolution of the substrate, chemical oxygen demand, dissolved organic carbon, toxicity and antimicrobial activity on Escherichia coli cultures were evaluated. The results indicate that, under optimal conditions, after 30 min, the TiO(2) photocatalytic system is able to eliminate both the substrate and the antimicrobial activity, and to reduce the toxicity of the solution by 60%. However, at the same time, ∼53% of both initial DOC and COD remain in solution. Thus, the photocatalytical system is able to transform the target compound into more oxidized by-products without antimicrobial activity and with a low toxicity. The study of OA by-products using liquid chromatography coupled with mass spectrometry, as well as the evaluation of OA degradation in acetonitrile media as solvent or in the presence of isopropanol and iodide suggest that the reaction is initiated by the photo-Kolbe reaction. Adsorption isotherm experiments in the dark indicated that under pH 7.5, adsorption corresponded to the Langmuir adsorption model, indicating the dependence of the reaction on an initial adsorption step.
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http://dx.doi.org/10.1016/j.watres.2010.05.011 | DOI Listing |
Water Res
January 2025
Faculty of Geosciences and Civil Engineering, Kanazawa University, Kanazawa 920-1192, Japan; Center for Infectious Disease Education and Research (CiDER), Osaka University, 565-0871, Japan. Electronic address:
Treated effluent of wastewater treatment plants (WWTPs) are major sources of extracellular antimicrobial resistance genes (eARGs) into aquatic environments. This study aimed to clarify the fate and origins of eARGs from influent to treated effluent at a full-scale WWTP. The compositions of eARG and intracellular ARG (iARG) were acquired via shotgun metagenomic sequencing in influent wastewater, activated sludge, and treated effluent of the target WWTP, where identical wastewater was treated by conventional activated sludge (CAS) and membrane bioreactor (MBR) processes.
View Article and Find Full Text PDFSci Adv
January 2025
Institut für Biologie und Biotechnologie der Pflanzen, Universität Münster, Münster, Germany.
Systemic signaling is an essential hallmark of multicellular life. Pathogen encounter occurs locally but triggers organ-scale and organismic immune responses. In plants, elicitor perception provokes systemically expanding Ca and HO signals conferring immunity.
View Article and Find Full Text PDFSci Adv
January 2025
Department of Chemistry, Stanford University, Stanford, CA 94305, USA.
Tigilanol tiglate (EBC-46) is a selective modulator of protein kinase C (PKC) isoforms that is Food and Drug Administration (FDA) approved for the treatment of mast cell tumors in canines with up to an 88% cure rate. Recently, it has been FDA approved for the treatment of soft tissue sarcomas in humans. The role of EBC-46 and, especially, its analogs in efforts to eradicate HIV, treat neurological and cardiovascular disorders, or enhance antigen density in antigen-targeted chimeric antigen receptor-T cell and chimeric antigen receptor-natural killer cell immunotherapies has not been reported.
View Article and Find Full Text PDFPLoS One
January 2025
Department of Pharmacognosy, Faculty of Pharmacy, Helwan University, Cairo, Egypt.
This study identifies the secondary metabolites from Alternaria alternate and evaluates their ACE-2: Spike RBD (SARS-CoV-2) inhibitory activity confirmed via immunoblotting in human lung microvascular endothelial cells. In addition, their in vitro anti-inflammatory potential was assessed using a cell-based assay in LPS-treated RAW 264.7 macrophage cells.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Division of Basic Science, Fred Hutchinson Cancer Center, Seattle, WA 98109.
Mx proteins, first identified in mammals, encode potent antiviral activity against a wide range of viruses. Mx proteins arose within the Dynamin superfamily of proteins (DSP), which mediate critical cellular processes, such as endocytosis and mitochondrial, plastid, and peroxisomal dynamics. Despite their crucial role, the evolutionary origins of Mx proteins are poorly understood.
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